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Yorodumi- PDB-9rvu: in situ S. pombe hibernating ribosome after 7 days of glucose dep... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9rvu | ||||||||||||||||||||||||||||||
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| Title | in situ S. pombe hibernating ribosome after 7 days of glucose depletion | ||||||||||||||||||||||||||||||
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Keywords | RIBOSOME / SNOR / pombe / Yeast / Hibernating / Glucose / Cryo-ET / in-situ | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationPeptide chain elongation / Hypusine synthesis from eIF5A-lysine / Synthesis of diphthamide-EEF2 / mTORC1-mediated signalling / Translation initiation complex formation / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / Platelet degranulation / Protein methylation / Protein hydroxylation ...Peptide chain elongation / Hypusine synthesis from eIF5A-lysine / Synthesis of diphthamide-EEF2 / mTORC1-mediated signalling / Translation initiation complex formation / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / Platelet degranulation / Protein methylation / Protein hydroxylation / regulation of cytoplasmic translational initiation in response to stress / RMTs methylate histone arginines / Neutrophil degranulation / Major pathway of rRNA processing in the nucleolus and cytosol / negative regulation of cell integrity MAPK cascade / positive regulation of conjugation with cellular fusion / L13a-mediated translational silencing of Ceruloplasmin expression / Formation of a pool of free 40S subunits / GTP hydrolysis and joining of the 60S ribosomal subunit / SRP-dependent cotranslational protein targeting to membrane / ribonuclease MRP complex / translational frameshifting / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / regulation of cytoplasmic translation / cytoplasmic translational elongation / GCN2-mediated signaling / positive regulation of translational termination / translation termination factor activity / translation activator activity / negative regulation of p38MAPK cascade / cytoplasmic translational termination / ribosome hibernation / positive regulation of translational elongation / preribosome / G-quadruplex DNA binding / tRNA processing / cytosolic large ribosomal subunit assembly / signaling receptor activator activity / negative regulation of translational frameshifting / ribosomal small subunit binding / TOR signaling / translational elongation / pre-mRNA intronic binding / ribosomal large subunit export from nucleus / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / translation elongation factor activity / protein-RNA complex assembly / maturation of LSU-rRNA / negative regulation of cytoplasmic translation / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / protein-membrane adaptor activity / positive regulation of autophagy / rescue of stalled cytosolic ribosome / protein kinase C binding / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / regulation of actin cytoskeleton organization / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / small-subunit processome / maintenance of translational fidelity / modification-dependent protein catabolic process / cytoplasmic stress granule / protein tag activity / rRNA processing / ribosomal small subunit assembly / ribosome biogenesis / ribosome binding / ribosomal small subunit biogenesis / 5S rRNA binding / small ribosomal subunit / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / structural constituent of ribosome / protein ubiquitination / ribosome / translation / ribonucleoprotein complex / negative regulation of gene expression / mRNA binding / GTPase activity / ubiquitin protein ligase binding / GTP binding / nucleolus / protein-containing complex / RNA binding / zinc ion binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 3.38 Å | ||||||||||||||||||||||||||||||
Authors | Rosa, H. / Gluc, M. / Jomaa, A. / Mattei, S. | ||||||||||||||||||||||||||||||
| Funding support | United States, Germany, 2items
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Citation | Journal: Nature / Year: 2026Title: SNOR promotes translation restart after dormancy. Authors: Maciej Gluc / Higor Rosa / Maria Bozko / Lesley A Turner / Cassidy R Prince / Yelena Peskova / Heather A Feaga / Kathleen L Gould / Simone Mattei / Ahmad Jomaa / ![]() Abstract: Cellular dormancy enables survival during prolonged nutrient limitation by reversibly suppressing protein synthesis. How inactive eukaryotic ribosomes are reactivated when nutrients return remains ...Cellular dormancy enables survival during prolonged nutrient limitation by reversibly suppressing protein synthesis. How inactive eukaryotic ribosomes are reactivated when nutrients return remains unclear. Here, using high-resolution in situ cryo-electron tomography in Schizosaccharomyces pombe, we identify SNOR, an SBDS domain-containing ribosome-associated factor that binds at the peptidyl transferase centre and contacts the hypusinated loop of eIF5A during glucose depletion-induced dormancy. Rather than acting as a canonical hibernation factor, SNOR licenses dormant ribosomes for rapid translational restart. Upon glucose repletion, SNOR and eIF5A act together to promote efficient recovery of polysomes and exit from dormancy. These findings define a stress-responsive ribosome restart module that couples carbon-source limitation to surveillance of the ribosomal active site and reactivation of protein synthesis. | ||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9rvu.cif.gz | 5.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9rvu.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9rvu.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rv/9rvu ftp://data.pdbj.org/pub/pdb/validation_reports/rv/9rvu | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 54290MC ![]() 9phcC C: citing same article ( M: map data used to model this data |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-RNA chain , 4 types, 4 molecules AAB2B3B4
| #1: RNA chain | Mass: 593528.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #36: RNA chain | Mass: 1129812.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #37: RNA chain | Mass: 78518.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #38: RNA chain | Mass: 52880.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+Small ribosomal subunit protein ... , 32 types, 32 molecules ADAEAFAGAHAIAJAKALAMANAOAPAQARASATAUAVAWAaAbAcAdAeAfAgAhAiAjAkAm
+Large ribosomal subunit protein ... , 43 types, 43 molecules B0B1BNBOBPBQBRBSBTBVBWBXBYBZBaBcBdBeBfBgBhBiBjBkBlBmBnBoBpBq...
-Protein , 4 types, 4 molecules H1HEHSHI
| #75: Protein | Mass: 31007.371 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #76: Protein | Mass: 93344.883 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #78: Protein | Mass: 11909.361 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #79: Protein | Mass: 17260.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 1 types, 6 molecules 
| #84: Chemical | ChemComp-ZN / |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: CELL / 3D reconstruction method: subtomogram averaging |
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Sample preparation
| Component | Name: In situ cryo-ET Hibernating Ribosome from S. pombe under 7-day glucose depletion conditions Type: RIBOSOME Details: Full hibernating ribosome (Large and Small Subunits) with eEF2, eIF5a (with hypusination), SNOR (SBDS-domain containing hibernation factor), and Stm1. Entity ID: #1-#83 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 5.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 300 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS / Details: Objective Aperture 70 um |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 4000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm / Alignment procedure: ZEMLIN TABLEAU |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 3.4 e/Å2 / Avg electron dose per subtomogram: 140 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
| EM imaging optics | Energyfilter name: TFS Selectris X / Energyfilter slit width: 10 eV |
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Processing
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| CTF correction | Details: 3D CTF Estimation done in Warp / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | |||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.38 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 88206 / Symmetry type: POINT | |||||||||||||||||||||||||
| EM volume selection | Num. of tomograms: 715 / Num. of volumes extracted: 95485 | |||||||||||||||||||||||||
| Refinement | Highest resolution: 3.38 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | |||||||||||||||||||||||||
| Refine LS restraints |
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